Advances in Bioactive Peptides from Natural Sources: Characterization, Biological Targets and Promising Applications

A special issue of Pharmaceutics (ISSN 1999-4923). This special issue belongs to the section "Biologics and Biosimilars".

Deadline for manuscript submissions: 20 November 2024 | Viewed by 4186

Special Issue Editors


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LAFMOL–Laboratory of Functional and Molecular Studies in Physiopharmacology, Department of Biophysics and Physiology, Federal University of Piauí, Teresina 64049-550, Brazil
Interests: bioactive peptides; cardiovascular; diabetes; dyslipidemia; endothelium; hypertension; medicinal plants; natural products; pharmacology; preclinical toxicology; vasorelaxant
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Research Center in Applied Morphology and Immunology (NuPMIA), Faculty of Medicine (FM), University of Brasília (UnB), Brasília 70910-900, DF, Brazil
Interests: biotechnology; bionanotechnology; bioprospection; biomolecules; health and environment
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LAQV/REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal
Interests: secondary metabolites; natural antioxidants; in vitro, in vivo, and in silico models; structure–activity relationship; natural product chemistry; oxidative stress and antioxidant defense; free-radical-mediated chain reactions; extraction and separation methods; antioxidant ingredients and biomaterials
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Venomous animals are considered specialized predators which have developed the most sophisticated apparatus regarding the chemistry and pharmacology of bioactive peptides, with a wide range of toxins with incredible structural and functional diversity and directed against a variety of pharmacological targets and with potential therapeutic applications. For example, studies on the pathophysiological mechanisms of envenoming and molecular characterization of toxins from the Bothrops jararaca snake venom resulted in the relevant discovery of bradykinin and bradykinin-potentiating peptides (BPPs), recognized by the first natural inhibitors of angiotensin I-converting enzyme (ACE) and model for the development of captopril, the first ACE inhibitor and the first commercially available drug for the treatment of arterial hypertension. In this sense, several peptides obtained from the venoms of amphibians, snakes, scorpions, and spiders have been reported in the literature as important bioactive compounds with important pharmacological effects and potential therapeutic applications. The aim of this Special Issue is to report current advances in bioactive peptides from natural sources, focusing on their characterization, biological targets, and promising applications. We are pleased to invite you to submit original research articles and reviews. Research areas may include (but are not limited to) the discovery and characterization of novel bioactive peptides, including pharmacological studies and development of bioproducts.

We look forward to receiving your contributions.

Dr. Daniel Arcanjo
Prof. Dr. José Roberto de Souza de Almeida Leite
Dr. Alexandra Plácido
Guest Editors

Manuscript Submission Information

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Keywords

  • bioactivity
  • synthesis
  • pharmacology
  • toxicology
  • immunogenicity
  • snake venom
  • scorpion venom
  • skin secretion
  • nanoparticles
  • bioassays

Published Papers (3 papers)

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Research

23 pages, 2791 KiB  
Article
An Effective Modification Strategy to Build Multifunctional Peptides Based on a Trypsin Inhibitory Peptide of the Kunitz Family
by Ying Wang, Daning Shi, Wanchen Zou, Yangyang Jiang, Tao Wang, Xiaoling Chen, Chengbang Ma, Wei Li, Tianbao Chen, James F. Burrows, Lei Wang and Mei Zhou
Pharmaceutics 2024, 16(5), 597; https://doi.org/10.3390/pharmaceutics16050597 - 27 Apr 2024
Viewed by 818
Abstract
Peptides with antimicrobial activity or protease inhibitory activity are potential candidates to supplement traditional antibiotics or cancer chemotherapies. However, the potential of many peptides are limited by drawbacks such as cytotoxicity or susceptibility to hydrolysis. Therefore, strategies to modify the structure of promising [...] Read more.
Peptides with antimicrobial activity or protease inhibitory activity are potential candidates to supplement traditional antibiotics or cancer chemotherapies. However, the potential of many peptides are limited by drawbacks such as cytotoxicity or susceptibility to hydrolysis. Therefore, strategies to modify the structure of promising peptides may represent an effective approach for developing more promising clinical candidates. In this study, the mature peptide OSTI−1949, a Kunitz-type inhibitor from Odorrana schmackeri, and four designed analogues were successfully synthesised. In contrast to the parent peptide, the analogues showed impressive multi-functionality including antimicrobial, anticancer, and trypsin inhibitory activities. In terms of safety, there were no obvious changes observed in the haemolytic activity at the highest tested concentration, and the analogue OSTI−2461 showed an increase in activity against cancer cell lines without cytotoxicity to normal cells (HaCaT). In summary, through structural modification of a natural Kunitz-type peptide, the biological activity of analogues was improved whilst retaining low cytotoxicity. The strategy of helicity enhancement by forming an artificial α-helix and ß-sheet structure provides a promising way to develop original bioactive peptides for clinical therapeutics. Full article
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18 pages, 4509 KiB  
Article
First Insights about Antiparasitic and Action Mechanisms of the Antimicrobial Peptide Hepcidin from Salmonids against Caligus rogercresseyi
by Paula A. Santana, Camila Arancibia, Laura Tamayo, Juan Pablo Cumillaf, Tanya Roman, Constanza Cárdenas, Cinthya Paillan Suarez, Claudio A. Álvarez and Fanny Guzman
Pharmaceutics 2024, 16(3), 378; https://doi.org/10.3390/pharmaceutics16030378 - 8 Mar 2024
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Abstract
Currently, one of the primary challenges in salmon farming is caligidosis, caused by the copepod ectoparasites Caligus spp. The infection process is determined by the copepod’s ability to adhere to the fish skin through the insertion of its chitin-composed filament. In this study, [...] Read more.
Currently, one of the primary challenges in salmon farming is caligidosis, caused by the copepod ectoparasites Caligus spp. The infection process is determined by the copepod’s ability to adhere to the fish skin through the insertion of its chitin-composed filament. In this study, we examined several antimicrobial peptides previously identified in salmonid mucosal secretions, with a primary focus on their potential to bind to chitin as an initial step. The binding capacity to chitin was tested, with hepcidin and piscidin showing positive results. Further assessments involving cytotoxicity in salmonid cells RTgill-W1, SHK-1, RTS-11, and RT-gut indicated that the peptides did not adversely affect cell viability. However, hemolysis assays unveiled the hemolytic capacity of piscidin at lower concentrations, leading to the selection of hepcidin for antiparasitic assays. The results demonstrated that the nauplius II stage of C. rogercresseyi exhibited higher susceptibility to hepcidin treatments, achieving a 50% reduction in parasitic involvement at 50 µM. Utilizing fluorescence and scanning electron microscopy, we observed the localization of hepcidin on the surface of the parasite, inducing significant spherical protuberances along the exoskeleton of C. rogercresseyi. These findings suggest that cysteine-rich AMPs derived from fish mucosa possess the capability to alter the development of the chitin exoskeleton in copepod ectoparasites, making them therapeutic targets to combat recurrent parasitic diseases in salmon farming. Full article
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19 pages, 4524 KiB  
Article
Antiviral Action against SARS-CoV-2 of a Synthetic Peptide Based on a Novel Defensin Present in the Transcriptome of the Fire Salamander (Salamandra salamandra)
by Ana Luisa A. N. Barros, Vladimir C. Silva, Atvaldo F. Ribeiro-Junior, Miguel G. Cardoso, Samuel R. Costa, Carolina B. Moraes, Cecília G. Barbosa, Alex P. Coleone, Rafael P. Simões, Wanessa F. Cabral, Raul M. Falcão, Andreanne G. Vasconcelos, Jefferson A. Rocha, Daniel D. R. Arcanjo, Augusto Batagin-Neto, Tatiana Karla S. Borges, João Gonçalves, Guilherme D. Brand, Lucio H. G. Freitas-Junior, Peter Eaton, Mariela Marani, Massuo J. Kato, Alexandra Plácido and José Roberto S. A. Leiteadd Show full author list remove Hide full author list
Pharmaceutics 2024, 16(2), 190; https://doi.org/10.3390/pharmaceutics16020190 - 29 Jan 2024
Cited by 1 | Viewed by 1527
Abstract
The potential emergence of zoonotic diseases has raised significant concerns, particularly in light of the recent pandemic, emphasizing the urgent need for scientific preparedness. The bioprospection and characterization of new molecules are strategically relevant to the research and development of innovative drugs for [...] Read more.
The potential emergence of zoonotic diseases has raised significant concerns, particularly in light of the recent pandemic, emphasizing the urgent need for scientific preparedness. The bioprospection and characterization of new molecules are strategically relevant to the research and development of innovative drugs for viral and bacterial treatment and disease management. Amphibian species possess a diverse array of compounds, including antimicrobial peptides. This study identified the first bioactive peptide from Salamandra salamandra in a transcriptome analysis. The synthetic peptide sequence, which belongs to the defensin family, was characterized through MALDI TOF/TOF mass spectrometry. Molecular docking assays hypothesized the interaction between the identified peptide and the active binding site of the spike WT RBD/hACE2 complex. Although additional studies are required, the preliminary evaluation of the antiviral potential of synthetic SS-I was conducted through an in vitro cell-based SARS-CoV-2 infection assay. Additionally, the cytotoxic and hemolytic effects of the synthesized peptide were assessed. These preliminary findings highlighted the potential of SS-I as a chemical scaffold for drug development against COVID-19, hindering viral infection. The peptide demonstrated hemolytic activity while not exhibiting cytotoxicity at the antiviral concentration. Full article
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